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P06971 (FHUA_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 132. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Ferrichrome-iron receptor
Alternative name(s):
Ferric hydroxamate receptor
Ferric hydroxamate uptake
Gene names
Name:fhuA
Synonyms:tonA
Ordered Locus Names:b0150, JW0146
OrganismEscherichia coli (strain K12)
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length747 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

This receptor binds the ferrichrome-iron ligand. It interacts with the TonB protein, which is responsible for energy coupling of the ferrichrome-promoted iron transport system. Acts as a receptor for bacteriophage T5 as well as T1, phi80 and colicin M. Binding of T5 triggers the opening of a high conductance ion channel. Can also transport the antibiotic albomycin. Ref.8

Subunit structure

Monomer.

Subcellular location

Cell outer membrane; Multi-pass membrane protein.

Sequence similarities

Belongs to the TonB-dependent receptor family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 3333 Ref.1
Chain34 – 747714Ferrichrome-iron receptor
PRO_0000034748

Regions

Topological domain34 – 192159Periplasmic
Transmembrane193 – 2019Beta stranded
Topological domain202 – 2065Extracellular
Transmembrane207 – 2159Beta stranded
Topological domain216 – 2227Periplasmic
Transmembrane223 – 2319Beta stranded
Topological domain232 – 24514Extracellular
Transmembrane246 – 25510Beta stranded
Topological domain256 – 2594Periplasmic
Transmembrane260 – 2689Beta stranded
Topological domain269 – 31244Extracellular
Transmembrane313 – 3219Beta stranded
Topological domain322 – 3265Periplasmic
Transmembrane327 – 3359Beta stranded
Topological domain336 – 38752Extracellular
Transmembrane388 – 3969Beta stranded
Topological domain397 – 4048Periplasmic
Transmembrane405 – 4139Beta stranded
Topological domain414 – 46451Extracellular
Transmembrane465 – 4739Beta stranded
Topological domain474 – 4774Periplasmic
Transmembrane478 – 4869Beta stranded
Topological domain487 – 50822Extracellular
Transmembrane509 – 5179Beta stranded
Topological domain518 – 5225Periplasmic
Transmembrane523 – 5319Beta stranded
Topological domain532 – 55120Extracellular
Transmembrane552 – 5609Beta stranded
Topological domain561 – 5655Periplasmic
Transmembrane566 – 5749Beta stranded
Topological domain575 – 60127Extracellular
Transmembrane602 – 6109Beta stranded
Topological domain611 – 6133Periplasmic
Transmembrane614 – 6229Beta stranded
Topological domain623 – 64523Extracellular
Transmembrane646 – 6549Beta stranded
Topological domain655 – 6617Periplasmic
Transmembrane662 – 6709Beta stranded
Topological domain671 – 68919Extracellular
Transmembrane690 – 6989Beta stranded
Topological domain699 – 7057Periplasmic
Transmembrane706 – 7149Beta stranded
Topological domain715 – 73723Extracellular
Transmembrane738 – 7469Beta stranded
Topological domain7471Periplasmic
Region148 – 1492Ferrichrome binding
Motif40 – 478TonB box
Motif730 – 74718TonB C-terminal box

Sites

Binding site1141Ferrichrome
Binding site1331Ferrichrome
Binding site2771Ferrichrome
Binding site2791Ferrichrome
Binding site3461Ferrichrome
Binding site3481Ferrichrome
Binding site4241Ferrichrome
Binding site7351Ferrichrome

Amino acid modifications

Disulfide bond351 ↔ 362
Disulfide bond725 ↔ 731

Experimental info

Sequence conflict609 – 6102AA → RP Ref.2
Sequence conflict7371R → P in CAA29253. Ref.6

Secondary structure

1 ...................................................................................................... 747
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P06971 [UniParc].

Last modified November 1, 1997. Version 2.
Checksum: 1C2B251D1990E444

FASTA74782,182
        10         20         30         40         50         60 
MARSKTAQPK HSLRKIAVVV ATAVSGMSVY AQAAVEPKED TITVTAAPAP QESAWGPAAT 

        70         80         90        100        110        120 
IAARQSATGT KTDTPIQKVP QSISVVTAEE MALHQPKSVK EALSYTPGVS VGTRGASNTY 

       130        140        150        160        170        180 
DHLIIRGFAA EGQSQNNYLN GLKLQGNFYN DAVIDPYMLE RAEIMRGPVS VLYGKSSPGG 

       190        200        210        220        230        240 
LLNMVSKRPT TEPLKEVQFK AGTDSLFQTG FDFSDSLDDD GVYSYRLTGL ARSANAQQKG 

       250        260        270        280        290        300 
SEEQRYAIAP AFTWRPDDKT NFTFLSYFQN EPETGYYGWL PKEGTVEPLP NGKRLPTDFN 

       310        320        330        340        350        360 
EGAKNNTYSR NEKMVGYSFD HEFNDTFTVR QNLRFAENKT SQNSVYGYGV CSDPANAYSK 

       370        380        390        400        410        420 
QCAALAPADK GHYLARKYVV DDEKLQNFSV DTQLQSKFAT GDIDHTLLTG VDFMRMRNDI 

       430        440        450        460        470        480 
NAWFGYDDSV PLLNLYNPVN TDFDFNAKDP ANSGPYRILN KQKQTGVYVQ DQAQWDKVLV 

       490        500        510        520        530        540 
TLGGRYDWAD QESLNRVAGT TDKRDDKQFT WRGGVNYLFD NGVTPYFSYS ESFEPSSQVG 

       550        560        570        580        590        600 
KDGNIFAPSK GKQYEVGVKY VPEDRPIVVT GAVYNLTKTN NLMADPEGSF FSVEGGEIRA 

       610        620        630        640        650        660 
RGVEIEAKAA LSASVNVVGS YTYTDAEYTT DTTYKGNTPA QVPKHMASLW ADYTFFDGPL 

       670        680        690        700        710        720 
SGLTLGTGGR YTGSSYGDPA NSFKVGSYTV VDALVRYDLA RVGMAGSNVA LHVNNLFDRE 

       730        740 
YVASCFNTYG CFWGAERQVV ATATFRF

« Hide

References

« Hide 'large scale' references
[1]"Protein fusions of beta-galactosidase to the ferrichrome-iron receptor of Escherichia coli K-12."
Coulton J.W., Mason P., Cameron D.R., Carmel G., Jean R., Rode H.N.
J. Bacteriol. 165:181-192(1986) [PubMed: 3079747] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 34-47.
Strain: K12.
[2]"Systematic sequencing of the Escherichia coli genome: analysis of the 2.4-4.1 min (110,917-193,643 bp) region."
Fujita N., Mori H., Yura T., Ishihama A.
Nucleic Acids Res. 22:1637-1639(1994) [PubMed: 8202364] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[3]"The complete genome sequence of Escherichia coli K-12."
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y.
Science 277:1453-1474(1997) [PubMed: 9278503] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / MG1655 / ATCC 47076.
[4]"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
Mol. Syst. Biol. 2:E1-E5(2006) [PubMed: 16738553] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], SEQUENCE REVISION TO 609-610.
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[5]"Sequence of minutes 4-25 of Escherichia coli."
Chung E., Allen E., Araujo R., Aparicio A.M., Davis K., Duncan M., Federspiel N., Hyman R., Kalman S., Komp C., Kurdi O., Lew H., Lin D., Namath A., Oefner P., Roberts D., Schramm S., Davis R.W.
Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] OF 482-647.
Strain: K12 / MG1655 / ATCC 47076.
[6]"Nucleotide sequence of the fhuC and fhuD genes involved in iron (III) hydroxamate transport: domains in FhuC homologous to ATP-binding proteins."
Burkhardt R., Braun V.
Mol. Gen. Genet. 209:49-55(1987) [PubMed: 2823072] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 723-747.
[7]"Energy-coupled transport through the outer membrane of Escherichia coli small deletions in the gating loop convert the FhuA transport protein into a diffusion channel."
Braun V., Killman H., Benz R.
FEBS Lett. 346:59-64(1994) [PubMed: 7515827] [Abstract]
Cited for: REVIEW.
[8]"FhuA, a transporter of the Escherichia coli outer membrane, is converted into a channel upon binding of bacteriophage T5."
Bonhivers M., Ghazi A., Boulanger P., Letellier L.
EMBO J. 15:1850-1856(1996) [PubMed: 8617231] [Abstract]
Cited for: FUNCTION AS A ION CHANNEL.
[9]"Siderophore-mediated iron transport: crystal structure of FhuA with bound lipopolysaccharide."
Ferguson A.D., Hofmann E., Coulton J.W., Diederichs K., Welte W.
Science 282:2215-2220(1998) [PubMed: 9856937] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 34-747.
[10]"Transmembrane signaling across the ligand-gated FhuA receptor: crystal structures of free and ferrichrome-bound states reveal allosteric changes."
Locher K.P., Rees B., Koebnik R., Mitschler A., Moulinier L., Rosenbusch J.P., Moras D.
Cell 95:771-778(1998) [PubMed: 9865695] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 53-747.
[11]"Crystal structure of the antibiotic albomycin in complex with the outer membrane transporter FhuA."
Ferguson A.D., Braun V., Fiedler H.-P., Coulton J.W., Diederichs K., Welte W.
Protein Sci. 9:956-963(2000) [PubMed: 10850805] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.95 ANGSTROMS) OF 34-747.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		M12486 Genomic DNA. Translation: AAB61768.1.
U00096 Genomic DNA. Translation: AAC73261.1.
AP009048 Genomic DNA. Translation: BAB96726.2.
U70214 Genomic DNA. Translation: AAB08580.1.
X05810 Genomic DNA. Translation: CAA29253.1.
PIRQRECFE. F64738.
RefSeqNP_414692.1. NC_000913.2.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1BY3X-ray2.74A34-747[»]
1BY5X-ray2.60A34-747[»]
1FCPX-ray2.70A52-747[»]
1FI1X-ray2.90A52-747[»]
1QFFX-ray2.70A34-747[»]
1QFGX-ray2.50A34-747[»]
1QJQX-ray2.95A34-747[»]
1QKCX-ray3.10A34-747[»]
2FCPX-ray2.50A34-747[»]
2GRXX-ray3.30A/B34-747[»]
ProteinModelPortalP06971.
SMRP06971. Positions 51-747.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP-9602N.
IntActP06971. 4 interactions.

Protein family/group databases

TCDB1.B.14.1.4. outer membrane receptor (OMR) family.

2D gel databases

2DBase-EcoliP06971.

Proteomic databases

PRIDEP06971.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBESCT00000003695; EBESCP00000003695; EBESCG00000003023.
EBESCT00000017522; EBESCP00000016813; EBESCG00000016578.
GeneID944856.
GenomeReviewsGene locus JW0146 in contig AP009048_GR.
Gene locus b0150 in contig U00096_GR.
KEGGecj:JW0146.
eco:b0150.
PATRIC32115409. VBIEscCol129921_0156.

Organism-specific databases

EchoBASEEB0298.
EcoGeneEG10302. fhuA.

Phylogenomic databases

eggNOGCOG1629.
GeneTreeEBGT00070000031718.
HOGENOMHBG564417.
OMAPANGYSK.
PhylomeDBP06971.
ProtClustDBPRK10044.

Enzyme and pathway databases

BioCycEcoCyc:EG10302-MONOMER.

Gene expression databases

GenevestigatorP06971.

Family and domain databases

InterProIPR012910. Plug.
IPR000531. TonB-dep_rcpt_b-brl.
IPR010916. TonB_box_CS.
IPR010917. TonB_rcpt_CS.
IPR010105. TonB_sidphr_rcpt.
[Graphical view]
Gene3DG3DSA:2.170.130.10. Plug. 1 hit.
G3DSA:2.40.170.20. TonB-dep_rcpt_b-brl. 1 hit.
KOK02014.
PfamPF07715. Plug. 1 hit.
PF00593. TonB_dep_Rec. 1 hit.
[Graphical view]
TIGRFAMsTIGR01783. TonB-siderophor. 1 hit.
PROSITEPS00430. TONB_DEPENDENT_REC_1. 1 hit.
PS01156. TONB_DEPENDENT_REC_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

DrugBankDB01296. Glucosamine.

Entry information

Entry nameFHUA_ECOLI
AccessionPrimary (citable) accession number: P06971
Secondary accession number(s): P71280, P75665
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1988
Last sequence update: November 1, 1997
Last modified: January 25, 2012
This is version 132 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents